| IED ID | IndEnz0002018765 |
| Enzyme Type ID | protease018765 |
| Protein Name |
Apolipophorins Retinoid- and fatty acid-binding glycoprotein Cleaved into: Apolipophorin-2 ApoL2 Apolipophorin II ApoLII ; Apolipophorin-1 ApoL1 Apolipophorin I ApoLI |
| Gene Name | apolpp Rfabg RfaBp CG11064 |
| Organism | Drosophila melanogaster (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
| Enzyme Sequence | MARMKYNIALIGILASVLLTIAVNAENACNLGCPKSDNGLLKYIPGNYYDYSFDSILTIGASSDVPNDSDDTSLKVSGSAKIFAKGNCGYTLQLSSVKVTNTKESVEKKILNSIQKPVQFTLVSGILEPQICSDSSDLDYSLNIKRAVVSLLQSGIEAEHEVDVFGMCPTHTSTSKVGNANIITKARNLNSCSHREQINSGLVSGKVNEKAGITSSLLLQANYIKESRIVNHLIENVQLTETYKFIGNTKRNSDISAKVVTILKLKNPSGTKANSPGTGSTVRSLIFQRPETYTSKNINALKTILSDLVDSTGDYVKKETAKKFVEFIRLLRQSDSETLLELAAFPHPNKVLARKVYLDGLFRTSTAESARVILKQLSKFDEKEKLLAILSLNIVKSVDKETLNQAASQLLPNAPKELYIAVGNLVAKYCLKNYCQGPEIDAISKKFSDGLKHCKPNTKREEERIVYILKGLGNAKSLSGNTVAALSECASTGRSNRIRVAALHAFSKVKCEETLQSKSLELLKNRNEDSELRIEAYLSAISCPNAEVANQISEIVNSETVNQVGGFISSNLKAIRDSTDVSRDQQKYHLANIRVTKTFPVDYRRYSFNNEVSYKLESLGVGASTDYQIIYSQHGFLPRSSRINVTTEFFGTNYNVFEASVRQENVEDVLEYYLGPKGLVNKDFDEIVKLIEVGNNGVAAGGRARRSIVDDVSKISKKYKMYGVKNVQDLNLDVSLKLFGSELAFLSLGDNIPSSLDDIINYFSTSFEKAKQELSSFEKQFSSHHLFLDTDLAYPTSIGVPLELVAQGFAATKVDLAVSLDINAILEQNWQKAKYRLKFVPSVDINANVQIGFNAQVLSTGLRVVSSAHSATGSDITVAVISDGEGFNVDLELPREKLELINFNVDTELYVAEQDKQKAIALKGNKKNKNSQPSEICFNQLELVGLNICIKSSTSLSEVQAGNGNVAERGLSVSEKFHLSRPFNFAVYLTTERKFTFKGIHTQEAFSQKWKLDYSTPGSKVSHDTTVVYELGNKPKTFSRLSFDNSQCHFAVEGGINNDKNELVVYGQYEQDKEIKKSKIGFSKNGNEYKPLIEIQDNNGISNSINGYHADGKIVVKKNSNNIERYNFENFQVSNSNNAHVAVNGWSDVGTNSLTSELRISLDHQTFLIKENLKLENGLYEAGFFINDEHSPENIYGSSIHLTIADQSYALKTNGKAAAWSIGSDGSFNFQKLADSNSARAGSLVENVEIQYKNKQVGGIKIMSNFDVNKMDVDVEISREQKIGSIIVKYESNQRHAQDYSLEASAKINKHSIDVISKCDFNGNVYVVDNSLVTSWGTLLSAKGEIGQRYSAQDININIQGNVQISGKDKVTQWILKVIGTPDKTNSDFRISRDTSELIKLTSESQHPQDKISFAKLNLIVKNQLTAKGEFRVAKNGKGDFTASIDTLKTEPKHKLEIESKFHIQSPKYDIDASLTLDGKRKVHLKSENTIEKLKFSTKNIGEANDKIIAFEANGSLKGELRGNGEIQGTFIFNAPDGRVIDGSINRKISTNAKSGLSQGNIDAQLSDTPFGSNKKRSISLIGKLDRLNTKTKEFSANSNLVYTAFNGEKSEISYQIKQQPNGDAKNIDFSLKAYGNPLPQPFEIAFALGDYSAQHAVVSITSKYGEIFSVSANGNYNNNQALEYGLQANIEIPKSTLKSLEINSHGKVLKSLIGNENAAYNVEFFLDSKTSLGQYARVNTVWNGTANDGSYDFEAQTNNMESPLKFNGKYHRKQTGNIKDGDLTGKQTYVLNAQYGAQYVKMDASLGYGAEKVDIAYVIDSSFDSVKDIKVNIRTFKPLDDSTYVVTALFKQTDKSYGLDTTFYHSAHKKGVDIRLDLLKEKPIIISSIAELLGDRKGKVLFEILNLADLDIKINSEASYVSIDEFYIIVNWSSKKLKLDGYELEARAQSKNIKIQLKNENGIIFSGTATYALKKELNKTIIDGQGKVQYQGKALSGNFKLTRQHFDFGTDREVGFSYTFMGNLGSKNGLGTLKITNKEFNTKFSVCEEKRQCTNLIVQSIVSIDEQKLDAVEHTTLIIVDLRDFGYPYEFELKSQNTRQGLKYQYHLDSFIITGNNFKYQFTANVQPTSSTIKLALPKRQILFETTQKIPADGSLFGRYEQTASFFIDKLQKPDDVARFSAIVDVTGTERVAFNANGKLKFEHPTIRPLSISGQLNGDVNQQIASAEVIFDIFRLPEQKVVGNSELRNSRSQNGFNIAYITTVKSAGLQFQYQINSNAAVDIEAHEYNIGLELNNGEIDVKAISFLNKEKFEISLSESNKHIIYIVGDFSKQNHYAKLNTKVQILDKNPIEITSEVQPNSAKIILKRQDFIDGTAEVKLGKEFKVDVIGSGKQLFNGRVALDATNFLQTNYFINEDHLNGFWHIVESEINKDSEYISENIKERLKKSRQVTDKIVKLAKEAGPDFSKLQGKLLDYKNDIVQELEADQSIAPIIDGIRTLFKKIAGIVDDINKAISEILEKAQKSIVDIYDKLQALWKDSLLKAWEDFIITVQKLISTLKTEFIKICTQSFKDLLSALEKYGPALKNYGKAIGEIVKPINDAAQEVIKIVVNAAEGVTHEFKQYVASLPSFESIRNEFNDKVKVLKLFEKATELTNSLFDQINILPQTPETSEFLQKLHDYLIAKLKQEHIDNEKYIEELGQLLIKAVRSIWVSIRSTYPGSSDHVIDFQSWIGSLTHSFDSLAVLPSILSFRSSILNCLLNENWDVVFNKKLLYSWIFFNDFELRGHVVDGKHIFTFDGLNFAYPGNCKYILAQDSVDNNFTIIGQLTNGKLKSITLIDREGSYFEVADNLALKLNGNLVEYPQHLSGLHAWRRFYTIHLYSEYGVGIVCTSDLKVCHININGFYTSKTRGLLGNGNAEPYDDFLLIDGTLAENSAALGNDYGVGKCTAIEFDNNQFKSSKRQEMCSELFGIESTLAFNFITLDSRPYRKACDIALAKVAEKEKEATACTFALAYGSAVKQINKWVLLPPRCIKCAGPAGQHDFGDEFTVKLPNNKVDVVFVVDINVTPGVLSNLIAPAINDIRESLRSRGFSDVQVGVIVFEETKRYPALLTSDGGKINYKGNVADVKLAGIKSFCDNCVEQIITEKRILDIYNSLKEIVKGIAPQADEKAFQLALDYPFRAGAAKSIIGVRSDSLEYKNWWKFVRAQLTGSITKFDGALIHLIAPVKGLSLEGVLSEKLIGFNSRLVATVDGKDSKKRTKLQFDNDMGIDFVLNNGGWVFATQNFEKLKASDQKKMLNQITSSLADTLFKTEIVSDCRCLPIHGLHGQHKCVIKSSTFVANKKAKSA |
| Enzyme Length | 3351 |
| Uniprot Accession Number | Q9V496 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Constitutes the major component of lipophorin, which mediates transport for various types of lipids in hemolymph. Acts by forming lipoprotein particles that bind lipoproteins and lipids. Also involved in the transport of hydrophobic ligands like juvenile hormones, pheromone hydrocarbons and carotenoids. Required for morphogens wingless (wg) and hedgehog (hh) function, probably by acting as vehicles for the movement of wg and hh, explaining how covalently lipidated wg and hh can spread over long distances. May also be involved in transport and/or metabolism of heme. {ECO:0000269|PubMed:15875013, ECO:0000269|PubMed:8702812}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Domain (2); Glycosylation (7); Natural variant (1); Sequence conflict (2); Signal peptide (1); Site (1) |
| Keywords | Cleavage on pair of basic residues;Direct protein sequencing;Glycoprotein;Heme;Iron;Lipid transport;Lipid-binding;Lipoprotein;Metal-binding;Reference proteome;Secreted;Signal;Transport;Wnt signaling pathway |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. Note=Secreted in hemolymph. |
| Modified Residue | |
| Post Translational Modification | PTM: May be modified covalently by lipidation. {ECO:0000269|PubMed:8031123}.; PTM: Cleaved into 2 chains by furin protease. However, prevention of cleavage does not impair its function (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000269|PubMed:8702812 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10880479; 11076973; 11404335; 12417656; 12594038; 12915459; 14605208; 14707262; 15094375; 15185094; 15219154; 15466469; 15640802; 15710747; 15736317; 16364628; 16816428; 17138665; 17344229; 17609110; 17728343; 18198278; 18245350; 18433294; 19154620; 19307603; 19502482; 19503609; 19545586; 19704789; 19906846; 19914231; 19951294; 20074523; 20220848; 20387871; 20530634; 20685986; 20813047; 20976106; 21074052; 21347279; 21447707; 21480662; 22000799; 22290933; 22430022; 22724070; 22844248; 23028361; 23132924; 23296921; 23352167; 23455472; 23545286; 23554573; 23626758; 23868318; 23944235; 24037266; 24535443; 24658702; 24807223; 25027439; 25242144; 25294943; 25471885; 25544350; 25565944; 25596379; 25733905; 25740935; 25953899; 26121667; 26173873; 26353752; 26468879; 26526100; 26801178; 26839216; 26896675; 26935105; 27357258; 27406568; 27582081; 28095410; 28280122; 28396508; 28669758; 29046397; 29486196; 29619822; 30559276; 30692666; 30995484; 31036678; 31422916; 31799578; 32344153; 32487456; 32598400; 32900993; 32901612; 32931938; 33006316; 33107824; 33355241; 33355243; 33526583; 33537463; 33891588; 33893307; 34082046; 34305631; 34644570; 8742826; 8994352; 9367652; 9878414; |
| Motif | |
| Gene Encoded By | |
| Mass | 372,677 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |